Publication

"Glass transition" in peptides: Temperature and pressure effects

2005
Journal Articles

Abstract

We report on the origin of the liquid-to-glass transition in a series of oligopeptides of γ -benzyl-L-glutamate up to the polymer (PBLG), and in Poly-Z-L-lysine (PZLL) and Polyglycine (PGly) using dielectric spectroscopy as a function of temperature and pressure. We show that temperature is the dominant control variable of the dynamics associated with the peptidic "glass transition." This is an intrinsic feature of the peptide dynamics, irrespective of the type of amino acid and of the peptide secondary structure. The influence of the type of secondary structure (α helix vs ß sheet) on the liquid-to-glass dynamics is discussed. © 2005 American Institute of Physics.

Official source

https://infoscience.epfl.ch/entities/publication/b0842ae9-2599-4666-8693-8fe1a67d33ec

About this result

This page is automatically generated and may contain information that is not correct, complete, up-to-date, or relevant to your search query. The same applies to every other page on this website. Please make sure to verify the information with EPFL's official sources.

Graph Chat

Chat with Graph Search

Ask any question about EPFL courses, lectures, exercises, research, news, etc. or try the example questions below.

DISCLAIMER: The Graph Chatbot is not programmed to provide explicit or categorical answers to your questions. Rather, it transforms your questions into API requests that are distributed across the various IT services officially administered by EPFL. Its purpose is solely to collect and recommend relevant references to content that you can explore to help you answer your questions.

2005
Journal Articles

Abstract

Official source

https://infoscience.epfl.ch/entities/publication/b0842ae9-2599-4666-8693-8fe1a67d33ec

About this result

Related concepts (32)

Protein structure

Protein structure is the three-dimensional arrangement of atoms in an amino acid-chain molecule. Proteins are polymers - specifically polypeptides - formed from sequences of amino acids, which are the monomers of the polymer. A single amino acid monomer may also be called a residue, which indicates a repeating unit of a polymer. Proteins form by amino acids undergoing condensation reactions, in which the amino acids lose one water molecule per reaction in order to attach to one another with a peptide bond.

Protein secondary structure

Protein secondary structure is the local spatial conformation of the polypeptide backbone excluding the side chains. The two most common secondary structural elements are alpha helices and beta sheets, though beta turns and omega loops occur as well. Secondary structure elements typically spontaneously form as an intermediate before the protein folds into its three dimensional tertiary structure. Secondary structure is formally defined by the pattern of hydrogen bonds between the amino hydrogen and carboxyl oxygen atoms in the peptide backbone.

Glass transition

The glass–liquid transition, or glass transition, is the gradual and reversible transition in amorphous materials (or in amorphous regions within semicrystalline materials) from a hard and relatively brittle "glassy" state into a viscous or rubbery state as the temperature is increased. An amorphous solid that exhibits a glass transition is called a glass. The reverse transition, achieved by supercooling a viscous liquid into the glass state, is called vitrification.

Related publications (14)

"Glass transition" in peptides: Temperature and pressure effects

Chat with Graph Search

Synthesis and pyroelectric response of disperse red 1 functionalized silicones: cyclic monomer, homopolymer, and block copolymer derivatives

Modeling of rough contact interfaces with trapped compressive liquid pockets

Improving binding affinity and stability of peptide ligands by substituting glycines with D-amino acids